ID   HYDMA_HYDVU             Reviewed;          84 AA.
AC   B3RFR8;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 29.
DE   RecName: Full=Hydramacin-1;
DE            Short=Hm-1;
DE   Flags: Precursor;
OS   Hydra vulgaris (Hydra) (Hydra attenuata).
OC   Eukaryota; Metazoa; Cnidaria; Hydrozoa; Hydroidolina; Anthoathecata;
OC   Aplanulata; Hydridae; Hydra.
OX   NCBI_TaxID=6087;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 39-50, FUNCTION,
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, PYROGLUTAMATE
RP   FORMATION AT GLN-25, AND MASS SPECTROMETRY.
RX   PubMed=19013190; DOI=10.1016/j.dci.2008.10.004;
RA   Bosch T.C.G., Augustin R., Anton-Erxleben F., Fraune S., Hemmrich G.,
RA   Zill H., Rosenstiel P., Jacobs G., Schreiber S., Leippe M., Stanisak M.,
RA   Groetzinger J., Jung S., Podschun R., Bartels J., Harder J.,
RA   Schroeder J.-M.;
RT   "Uncovering the evolutionary history of innate immunity: the simple
RT   metazoan Hydra uses epithelial cells for host defence.";
RL   Dev. Comp. Immunol. 33:559-569(2009).
RN   [2]
RP   STRUCTURE BY NMR OF 25-84, DISULFIDE BONDS, FUNCTION, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=19019828; DOI=10.1074/jbc.m804713200;
RA   Jung S., Dingley A.J., Augustin R., Anton-Erxleben F., Stanisak M.,
RA   Gelhaus C., Gutsmann T., Hammer M.U., Podschun R., Bonvin A.M.J.J.,
RA   Leippe M., Bosch T.C.G., Grotzinger J.;
RT   "Hydramacin-1, structure and antibacterial activity of a protein from the
RT   basal metazoan Hydra.";
RL   J. Biol. Chem. 284:1896-1905(2009).
CC   -!- FUNCTION: Cationic antimicrobial peptide potently active against Gram-
CC       positive and Gram-negative bacteria including multi-resistant human
CC       pathogenic strains. Is not active against the Gram-positive Coccus
CC       species, Gram-negative non-fermentation species and against the fungus
CC       C.albicans. It leads to aggregation of bacteria as an initial step of
CC       its bactericidal mechanism. Aggregated cells are connected via
CC       electron-dense contacts and adopt a thorn apple-like morphology.
CC       Hydramycin contains a belt of positively charged residues that separate
CC       two hydrophobic areas. This structure may explain the observed
CC       aggregation of bacteria, since each of these areas can immerse into the
CC       outer leaflets of the membranes of two individual bacteria. Is able to
CC       permeabilize membranes of viable bacteria at low and neutral pH values,
CC       but no pore-forming activity is not detected.
CC       {ECO:0000269|PubMed:19013190, ECO:0000269|PubMed:19019828}.
CC   -!- SUBCELLULAR LOCATION: Secreted. Target cell membrane.
CC   -!- TISSUE SPECIFICITY: Expressed in the endodermal epithelium.
CC       {ECO:0000269|PubMed:19013190}.
CC   -!- INDUCTION: By bacterial lipopolysaccharides (LPS).
CC       {ECO:0000269|PubMed:19013190}.
CC   -!- MASS SPECTROMETRY: Mass=6994; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:19013190};
CC   -!- SIMILARITY: Belongs to the macin family. {ECO:0000305}.
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DR   EMBL; DQ449931; ABE26989.1; -; mRNA.
DR   EMBL; CX833582; -; NOT_ANNOTATED_CDS; mRNA.
DR   PDB; 2K35; NMR; -; A=25-84.
DR   PDBsum; 2K35; -.
DR   AlphaFoldDB; B3RFR8; -.
DR   BMRB; B3RFR8; -.
DR   SMR; B3RFR8; -.
DR   EvolutionaryTrace; B3RFR8; -.
DR   Proteomes; UP000694840; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.30.100; -; 1.
DR   InterPro; IPR029230; Macin.
DR   InterPro; IPR038456; Macin_sf.
DR   Pfam; PF14865; Macin; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Antibiotic; Antimicrobial; Direct protein sequencing;
KW   Disulfide bond; Immunity; Innate immunity; Membrane;
KW   Pyrrolidone carboxylic acid; Reference proteome; Secreted; Signal;
KW   Target cell membrane; Target membrane.
FT   SIGNAL          1..24
FT   CHAIN           25..84
FT                   /note="Hydramacin-1"
FT                   /id="PRO_0000394509"
FT   MOD_RES         25
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000269|PubMed:19013190"
FT   DISULFID        29..72
FT                   /evidence="ECO:0000269|PubMed:19019828"
FT   DISULFID        36..65
FT                   /evidence="ECO:0000269|PubMed:19019828"
FT   DISULFID        51..81
FT                   /evidence="ECO:0000269|PubMed:19019828"
FT   DISULFID        55..83
FT                   /evidence="ECO:0000269|PubMed:19019828"
FT   STRAND          30..32
FT                   /evidence="ECO:0007829|PDB:2K35"
FT   HELIX           33..38
FT                   /evidence="ECO:0007829|PDB:2K35"
FT   TURN            41..44
FT                   /evidence="ECO:0007829|PDB:2K35"
FT   HELIX           50..56
FT                   /evidence="ECO:0007829|PDB:2K35"
FT   TURN            57..59
FT                   /evidence="ECO:0007829|PDB:2K35"
FT   STRAND          63..67
FT                   /evidence="ECO:0007829|PDB:2K35"
FT   HELIX           69..71
FT                   /evidence="ECO:0007829|PDB:2K35"
FT   TURN            75..77
FT                   /evidence="ECO:0007829|PDB:2K35"
FT   STRAND          79..83
FT                   /evidence="ECO:0007829|PDB:2K35"
SQ   SEQUENCE   84 AA;  9651 MW;  414E74FA879D791A CRC64;
     MRTVVFFILV SIFLVALKPT GTQAQIVDCW ETWSRCTKWS QGGTGTLWKS CNDRCKELGR
     KRGQCEEKPS RCPLSKKAWT CICY